SAPF_ECOLI
ID SAPF_ECOLI Reviewed; 268 AA.
AC P0AAH8; P36637;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putrescine export system ATP-binding protein SapF {ECO:0000303|PubMed:27803167};
GN Name=sapF; OrderedLocusNames=b1290, JW1283;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bergler H., Ebeling A., Fuchsbichler S., Hogenauer G., Turnowsky F.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / FRAG5;
RX PubMed=11700350; DOI=10.1099/00221287-147-11-2991;
RA Harms C., Domoto Y., Celik C., Rahe E., Stumpe S., Schmid R., Nakamura T.,
RA Bakker E.P.;
RT "Identification of the ABC protein SapD as the subunit that confers ATP
RT dependence to the K+-uptake systems Trk(H) and Trk(G) from Escherichia coli
RT K-12.";
RL Microbiology 147:2991-3003(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION IN PUTRESCINE EXPORT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=27803167; DOI=10.1074/jbc.m116.762450;
RA Sugiyama Y., Nakamura A., Matsumoto M., Kanbe A., Sakanaka M., Higashi K.,
RA Igarashi K., Katayama T., Suzuki H., Kurihara S.;
RT "A novel putrescine exporter SapBCDF of Escherichia coli.";
RL J. Biol. Chem. 291:26343-26351(2016).
CC -!- FUNCTION: Part of a putrescine export transport system, does not play a
CC role in resistance to antimicrobial peptides (PubMed:27803167). Does
CC not stimulate K(+) uptake ability of TrkH on its own, but increases
CC K(+) uptake by 20% in the presence of SapD; has no effect of TrkG
CC (PubMed:11700350). {ECO:0000269|PubMed:11700350,
CC ECO:0000269|PubMed:27803167}.
CC -!- INTERACTION:
CC P0AAH8; P0A9U3: ybiT; NbExp=2; IntAct=EBI-558765, EBI-558999;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Single mutation, decreased extracellular
CC putrescine, in an sapBCDF operon deletion no change in resistance to
CC antimicrobial peptide LL-37. {ECO:0000269|PubMed:27803167}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U08190; AAA17671.1; -; Unassigned_DNA.
DR EMBL; X97282; CAA65941.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74372.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14843.1; -; Genomic_DNA.
DR PIR; E64877; E64877.
DR RefSeq; NP_415806.1; NC_000913.3.
DR RefSeq; WP_000573407.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P0AAH8; -.
DR SMR; P0AAH8; -.
DR BioGRID; 4263241; 410.
DR BioGRID; 849711; 2.
DR ComplexPortal; CPX-4422; Putative peptide ABC transporter.
DR DIP; DIP-35903N; -.
DR IntAct; P0AAH8; 10.
DR STRING; 511145.b1290; -.
DR TCDB; 3.A.1.5.42; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AAH8; -.
DR PaxDb; P0AAH8; -.
DR PRIDE; P0AAH8; -.
DR EnsemblBacteria; AAC74372; AAC74372; b1290.
DR EnsemblBacteria; BAA14843; BAA14843; BAA14843.
DR GeneID; 66674883; -.
DR GeneID; 945335; -.
DR KEGG; ecj:JW1283; -.
DR KEGG; eco:b1290; -.
DR PATRIC; fig|1411691.4.peg.989; -.
DR EchoBASE; EB2211; -.
DR eggNOG; COG4172; Bacteria.
DR HOGENOM; CLU_000604_1_23_6; -.
DR InParanoid; P0AAH8; -.
DR OMA; NPLFTIQ; -.
DR PhylomeDB; P0AAH8; -.
DR BioCyc; EcoCyc:SAPF-MON; -.
DR BioCyc; MetaCyc:SAPF-MON; -.
DR BRENDA; 7.6.2.11; 2026.
DR PRO; PR:P0AAH8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0015489; F:putrescine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015833; P:peptide transport; IC:ComplexPortal.
DR GO; GO:0015847; P:putrescine transport; IMP:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..268
FT /note="Putrescine export system ATP-binding protein SapF"
FT /id="PRO_0000092968"
FT DOMAIN 6..251
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 268 AA; 30571 MW; F3B98BC9DC6DCBFA CRC64;
MIETLLEVRN LSKTFRYRTG WFRRQTVEAV KPLSFTLREG QTLAIIGENG SGKSTLAKML
AGMIEPTSGE LLIDDHPLHF GDYSFRSQRI RMIFQDPSTS LNPRQRISQI LDFPLRLNTD
LEPEQRRKQI IETMRMVGLL PDHVSYYPHM LAPGQKQRLG LARALILRPK VIIADEALAS
LDMSMRSQLI NLMLELQEKQ GISYIYVTQH IGMMKHISDQ VLVMHQGEVV ERGSTADVLA
SPLHELTKRL IAGHFGEALT ADAWRKDR
